Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding.
Journal Article (Journal Article)
By using Tb3+ as a luminescent probe, we demonstrate that the phosphorylation state of a 14-residue peptide fragment of alpha-synuclein, a protein implicated in Parkinson's Disease, dramatically affects the metal ion affinity of the peptide. Whereas the unphosphorylated peptide and its phosphoserine analogue show weak Tb3+ binding, its phosphotyrosine analogue shows tight 1:1 binding as well as 2:1 and 3:1 Tb:peptide adducts. Our data suggest that the phosphorylated amino acid must be appropriately positioned among additional ligating residues to establish this phosphorylation-dependent metal binding.
Full Text
Duke Authors
Cited Authors
- Liu, LL; Franz, KJ
Published Date
- July 2005
Published In
Volume / Issue
- 127 / 27
Start / End Page
- 9662 - 9663
PubMed ID
- 15998051
Electronic International Standard Serial Number (EISSN)
- 1520-5126
International Standard Serial Number (ISSN)
- 0002-7863
Digital Object Identifier (DOI)
- 10.1021/ja043247v
Language
- eng